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1E3Z

Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP231

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU261

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40
ChainResidueDetails
AASN102
AALA181
AASP202
AASP204
AHIS235

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10924103, ECO:0007744|PDB:1E40
ChainResidueDetails
AASP159
AASP183
AASP194
AASP200

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:20124706, ECO:0007744|PDB:3BH4
ChainResidueDetails
AGLY300

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
ChainResidueDetails
AASP407
AASP430
ATYR302
AHIS406

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP328

218853

PDB entries from 2024-04-24

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